Complete resolution of the solid-state NMR spectrum of a uniformly 15N-labeled membrane protein in phospholipid bilayers. Proc Natl Acad Sci U S A 1997 Aug 05;94(16):8551-6
Date
08/05/1997Pubmed ID
9238014Pubmed Central ID
PMC23006DOI
10.1073/pnas.94.16.8551Scopus ID
2-s2.0-0030844584 (requires institutional sign-in at Scopus site) 199 CitationsAbstract
Complete resolution of the amide resonances in a three-dimensional solid-state NMR correlation spectrum of a uniformly 15N-labeled membrane protein in oriented phospholipid bilayers is demonstrated. The three orientationally dependent frequencies, 1H chemical shift, 1H-15N dipolar coupling, and 15N chemical shift, associated with each amide resonance are responsible for resolution among resonances and provide sufficient angular restrictions for protein structure determination. Because the protein is completely immobilized by the phospholipids on the relevant NMR time scales (10 kHz), the linewidths will not degrade in the spectra of larger proteins. Therefore, these results demonstrate that solid-state NMR experiments can overcome the correlation time problem and extend the range of proteins that can have their structures determined by NMR spectroscopy to include uniformly 15N-labeled membrane proteins in phospholipid bilayers.
Author List
Marassi FM, Ramamoorthy A, Opella SJAuthor
Francesca M. Marassi PhD Chair, Professor in the Biophysics department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
Amino Acid SequenceEscherichia coli
Lipid Bilayers
Magnetic Resonance Spectroscopy
Membrane Proteins
Molecular Sequence Data
Phospholipids
Protein Binding
